ID C7M297_ACIFD Unreviewed; 451 AA.
AC C7M297;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACU54886.1};
GN OrderedLocusNames=Afer_1983 {ECO:0000313|EMBL:ACU54886.1};
OS Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS ICP).
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU54886.1, ECO:0000313|Proteomes:UP000000771};
RN [1] {ECO:0000313|EMBL:ACU54886.1, ECO:0000313|Proteomes:UP000000771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP
RC {ECO:0000313|Proteomes:UP000000771};
RX PubMed=21304635; DOI=10.4056/sigs.1463;
RA Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT (ICP).";
RL Stand. Genomic Sci. 1:38-45(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP001631; ACU54886.1; -; Genomic_DNA.
DR RefSeq; WP_015799362.1; NC_013124.1.
DR AlphaFoldDB; C7M297; -.
DR STRING; 525909.Afer_1983; -.
DR GeneID; 80815941; -.
DR KEGG; afo:Afer_1983; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_0_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000000771; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACU54886.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000771};
KW Transferase {ECO:0000313|EMBL:ACU54886.1}.
SQ SEQUENCE 451 AA; 48083 MW; 69BBF9601917F039 CRC64;
MTLVDRDRLG ALLADEAERF RASHPVSAQL ASRRGEHLVG GVPMTWMRRW ATPFAITVER
AKGSELVDVD GHRYLDVCLG DTGAMAGHSP EPTARAIRAR LESGGLTTML PTDDAEVVAD
ELTRRFGVER WQFTLSATDA NRFMLRTARQ LTKRPLVVVM DWCYHGTVDE SFVVLDGALT
RSRPGNVGPA VDPATTTRAV PFNDLGALEA ALADRQVAAV LTEPALTNIG IVLPDEGYLE
GLVELAHHYG SLVVLDETHT ISAGPGGLTG KLGLRPDGVT IGKAIGGGVP IGAWGLRAEL
ADAIVADRDA DLEDTGGIGG TLAGNALSLA AARATLTEVL TERAFDEMGA VSHELVRRER
ALLADHGFDW SVVELGARSE VRFVSPPPRT GADSARAADV DLDRYLHLAL ANREVLLTPF
HAMTLVAPTT TLAHVETYLD ALADALAPLA R
//
